Some properties of inorganic pyrophosphatase from Bacillus subtilis

被引：9

作者：

Shimizu, T

Imai, M

Araki, S

Kishida, K

Terasawa, Y

Hachimori, A

机构：

[1] SHINSHU UNIV,FAC TEXT SCI & TECHNOL,INST HIGH POLYMER RES,UEDA,NAGANO 386,JAPAN

[2] AIWA CO LTD,OKAYA,NAGANO 394,JAPAN

[3] ASAHIMATSU FOODS CO LTD,FOOD RES LAB,IIDA,NAGANO 39925,JAPAN

[4] OBUSEDO CORP,OBUSE,NAGANO 38102,JAPAN

[5] NAGANO DENPA,SHINONOI,NAGANO 38122,JAPAN

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 1997年 / 29卷 / 02期

关键词：

Bacillus subtilis; inorganic pyrophosphatase; thermostability;

D O I：

10.1016/S1357-2725(96)00088-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1; PPase) from Bacillus subtilis was purified to a homogeneous state electrophoretically when analysed by SDS-PAGE. The enzyme consists of six identical subunits; the molecular weight of the native enzyme estimated by gel filtration was approx. 120 000, and denaturing polyacrylamide gel electrophoresis gave a single band corresponding to 24 000. The enzyme absolutely required a divalent cation for its activity. Mg2+ was most effective, showing two steps of concentration-dependent activation. Mg2+ could be partially replaced by Mn2+ and Co2+. The enzyme was thermostable in the presence of Mg2+, and no loss of activity was observed on the incubation at 55 degrees C for an hour. (C) 1997 Elsevier Science Ltd.

引用

页码：303 / 310

页数：8